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Sodium in PDB 5zmw: Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg)

Enzymatic activity of Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg)

All present enzymatic activity of Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg):
3.6.3.8;

Protein crystallography data

The structure of Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg), PDB code: 5zmw was solved by H.Ogawa, A.Hirata, J.Tsueda, C.Toyoshima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.93 / 2.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 260.977, 86.895, 60.211, 90.00, 90.00, 90.00
R / Rfree (%) 22.2 / 25.9

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg) (pdb code 5zmw). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg), PDB code: 5zmw:

Sodium binding site 1 out of 1 in 5zmw

Go back to Sodium Binding Sites List in 5zmw
Sodium binding site 1 out of 1 in the Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of the E309Q Mutant of Sr CA2+-Atpase in E2(Tg) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1001

b:42.7
occ:1.00
O A:LEU711 2.5 18.3 1.0
O A:HOH1245 2.6 54.3 1.0
O A:ALA714 2.7 31.7 1.0
OE1 A:GLU732 2.7 44.5 1.0
O A:LYS712 2.7 31.6 1.0
O A:HOH1115 2.7 31.3 1.0
C A:LYS712 3.2 24.5 1.0
OE2 A:GLU732 3.2 40.2 1.0
CD A:GLU732 3.2 38.7 1.0
CA A:LYS712 3.4 23.3 1.0
C A:LEU711 3.5 30.3 1.0
O A:HOH1189 3.7 62.6 1.0
C A:ALA714 3.8 31.0 1.0
N A:LYS712 3.9 21.6 1.0
N A:ALA714 4.0 28.1 1.0
N A:LYS713 4.1 29.6 1.0
O A:HOH1324 4.2 66.3 1.0
O A:ALA730 4.2 42.1 1.0
N A:GLY717 4.2 31.7 1.0
C A:LYS713 4.3 31.4 1.0
CA A:ALA714 4.4 25.1 1.0
O A:HOH1207 4.5 62.9 1.0
O A:GLU715 4.6 35.4 1.0
CG A:GLU732 4.6 26.2 1.0
CA A:GLY717 4.7 24.8 1.0
O A:HOH1149 4.7 54.1 1.0
CA A:LYS713 4.7 32.3 1.0
O A:LYS713 4.7 32.7 1.0
CB A:LYS712 4.7 31.5 1.0
C A:GLU715 4.8 20.0 1.0
CA A:LEU711 4.9 30.9 1.0
CB A:ALA714 4.9 10.3 1.0
N A:GLU715 4.9 23.1 1.0

Reference:

N.Tsunekawa, H.Ogawa, J.Tsueda, T.Akiba, C.Toyoshima. Mechanism of the E2 to E1 Transition in CA2+Pump Revealed By Crystal Structures of Gating Residue Mutants. Proc. Natl. Acad. Sci. V. 115 12722 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30482857
DOI: 10.1073/PNAS.1815472115
Page generated: Tue Oct 8 01:32:01 2024

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